diff --git a/.gitlab-ci.yml b/.gitlab-ci.yml
index d53188a5be62226570bce0458c6062f1ab7d667b..9fd01a308b4556bb00d617623068afc9734154d7 100644
--- a/.gitlab-ci.yml
+++ b/.gitlab-ci.yml
@@ -39,6 +39,7 @@ stages:
   - update-meilisearch-indexes
   - get-meili-key
   - build
+  - build-wiki
   - deploy
 
 
@@ -352,6 +353,29 @@ build:prod:wiki:
     - if: $CI_COMMIT_BRANCH == "main"  
 
 
+
+build-wiki:
+  stage: build-wiki
+  image: node:21.1-bookworm-slim
+  variables:
+    NODE_OPTIONS: --max_old_space_size=12288
+    NUXT_APP_BASE_URL: /wiki/
+    NUXT_PUBLIC_MEILISEARCH_CLIENT_HOST_URL: ${MEILI_HOST}
+    NUXT_PUBLIC_MEILISEARCH_CLIENT_SEARCH_API_KEY: ${MEILI_API_KEY}
+    NUXT_PUBLIC_MEILI_HOST: ${MEILI_HOST}
+    NUXT_PUBLIC_MEILI_API_KEY: ${MEILI_API_KEY}
+  before_script:
+    - npm install
+  script:
+    - npm run generate
+  artifacts:
+    paths:
+      - .output/public
+
+
+
+
+
 ################ DEPLOY ##########################
 .deploy:
   stage: deploy
diff --git a/components/ServerDbTable.vue b/components/ServerDbTable.vue
index af1868ab752408a58667a4e35455c592e25a5fe0..4850583886fa8991795d8593645e192358e19bd7 100644
--- a/components/ServerDbTable.vue
+++ b/components/ServerDbTable.vue
@@ -132,7 +132,7 @@ const hasPlddt = computed(() => props.db === 'structure')
 // Fetch results
 const plddtFilter = computed(() => {
     const plddtRangeValue = plddtRange.value
-    if (hasPlddt.value && plddtRangeValue?.length === 2 && plddtRangeValue[0] !== 0 && plddtRangeValue[1] !== 100) {
+    if (hasPlddt.value && plddtRangeValue?.length === 2 && (plddtRangeValue[0] !== 0 || plddtRangeValue[1] !== 100)) {
         return `plddts ${plddtRangeValue[0]} TO ${plddtRangeValue[1]}`
     } else {
         return undefined
diff --git a/components/content/RefseqDb.vue b/components/content/RefseqDb.vue
index 48b40b0c31bc87f82b782fd7c28ca35b9dcfe360..ee4e713bbcd0f8a247d5283afe1a40fa7230f3a9 100644
--- a/components/content/RefseqDb.vue
+++ b/components/content/RefseqDb.vue
@@ -79,9 +79,6 @@ onMounted(async () => {
 })
 
 async function getAllHits(params) {
-    console.log("refresh hits")
-    console.log(params)
-    console.log(params.index)
     if (params.index === 'refseq') {
         console.log(params.index)
         const { data, error } = await useAsyncMeiliSearch(params)
@@ -189,7 +186,10 @@ function namesToCollapsibleChips(names: string[]) {
 
 function namesToAccessionChips(names: string[]) {
     return namesToCollapsibleChips(names).map(it => {
-        return { ...it, href: new URL(it.title, "http://toto.pasteur.cloud").toString() }
+        return {
+            ...it,
+            // href: new URL(it.title, "http://toto.pasteur.cloud").toString()
+        }
     })
 }
 const systemPanel: Ref<number> = ref(["table"])
@@ -226,34 +226,6 @@ const scaleType = ref("linear")
 
 <template>
     <v-card flat class="mb-2" color="transparent">
-        <v-toolbar>
-            <!-- <v-toolbar-title>Plots</v-toolbar-title> -->
-            <v-btn-toggle v-model="layoutPlot" density="compact" rounded="false" variant="text" color="primary" mandatory
-                class="mx-2">
-                <v-btn icon="md:grid_view" value="grid"></v-btn>
-                <v-btn icon="md:view_agenda" value="fullwidth"></v-btn>
-            </v-btn-toggle>
-            <v-spacer></v-spacer>
-            <v-select v-model="selectedTaxoRank" :items="availableTaxo" density="compact" label="Select taxonomic rank"
-                hide-details="auto" class="mx-2"></v-select>
-
-
-            <!-- <v-btn-toggle v-model="scaleTransform" density="compact" mandatory rounded="false" variant="text"
-                color="primary" class="mx-2">
-                <v-btn icon="mdi-math-log" value="linear">linear</v-btn>
-                <v-btn value="pow">pow</v-btn>
-                <v-btn icon="mdi-math-log" value="sqrt">sqrt</v-btn>
-                <v-btn icon="mdi-math-log" value="symlog">symlog</v-btn>
-                <v-btn icon="mdi-math-log" value="log">log</v-btn>
-            </v-btn-toggle> -->
-
-            <v-select v-model="scaleType" class="mx-2" density="compact" :items="['linear', 'sqrt', 'symlog']"
-                label="Scale Type" hide-details="auto"></v-select>
-
-
-        </v-toolbar>
-
-
         <v-card color="transparent" flat>
             <v-expansion-panels v-model="systemPanel" class="my-2" density="compact" multiple>
                 <v-expansion-panel elevation="3" value="barplot">
@@ -261,7 +233,18 @@ const scaleType = ref("linear")
                             class="mr-2">mdi-chart-bar</v-icon>Systems - Taxonomic</v-expansion-panel-title>
                     <v-expansion-panel-text>
                         <v-card flat color="transparent">
-
+                            <v-toolbar flat color="transparent" density="compact">
+                                <v-btn-toggle v-model="layoutPlot" density="compact" rounded="false" variant="text"
+                                    color="primary" mandatory class="mx-2">
+                                    <v-btn icon="md:grid_view" value="grid"></v-btn>
+                                    <v-btn icon="md:view_agenda" value="fullwidth"></v-btn>
+                                </v-btn-toggle>
+                                <v-select v-model="scaleType" class="mx-2" density="compact"
+                                    :items="['linear', 'sqrt', 'symlog']" label="Scale Type" hide-details="auto"></v-select>
+                                <v-select v-model="selectedTaxoRank" :items="availableTaxo" density="compact"
+                                    label="Select taxonomic rank" hide-details="auto" class="mx-2"></v-select>
+
+                            </v-toolbar>
                             <v-row align="start">
                                 <v-col :cols="fullWidth ? 12 : 6">
                                     <PlotFigure :options="unref(computedDistriSystemOptions)" defer></PlotFigure>
@@ -282,34 +265,37 @@ const scaleType = ref("linear")
                             class="mr-2">mdi-data-matrix</v-icon>Heatmap</v-expansion-panel-title>
                     <v-expansion-panel-text>
                         <v-card flat color="transparent">
+                            <v-toolbar flat color="transparent" density="compact">
+                                <v-select v-model="scaleType" class="mx-2" density="compact"
+                                    :items="['linear', 'sqrt', 'symlog']" label="Scale Type" hide-details="auto"></v-select>
+                                <v-select v-model="selectedTaxoRank" :items="availableTaxo" density="compact"
+                                    label="Select taxonomic rank" hide-details="auto" class="mx-2"></v-select>
+
+                            </v-toolbar>
                             <PlotFigure v-if="toValue(binPlotDataOptions) !== null" :options="unref(binPlotDataOptions)"
                                 defer>
                             </PlotFigure>
                         </v-card>
                     </v-expansion-panel-text>
                 </v-expansion-panel>
-                <v-expansion-panel elevation="3" value="table">
-                    <v-expansion-panel-title color="grey-lighten-4"><v-icon color="primary"
-                            class="mr-2">mdi-table</v-icon>Table</v-expansion-panel-title>
-                    <v-expansion-panel-text>
-                        <ServerDbTable title="RefSeq" db="refseq" :sortBy="sortBy" :facets="facets"
-                            :data-table-server-props="dataTableServerProps" @refresh:search="getAllHits">
-                            <template #top>
-                                <v-toolbar><v-toolbar-title class="text-capitalize">
-                                        RefSeq
-                                    </v-toolbar-title><v-spacer></v-spacer>
-
-                                </v-toolbar>
-                            </template>
-                            <template #[`item.accession_in_sys`]="{ item }">
-                                <CollapsibleChips :items="namesToAccessionChips(item.accession_in_sys)">
-                                </CollapsibleChips>
-                            </template>
-                        </ServerDbTable>
-                    </v-expansion-panel-text>
-                </v-expansion-panel>
             </v-expansion-panels>
 
+            <ServerDbTable title="RefSeq" db="refseq" :sortBy="sortBy" :facets="facets"
+                :data-table-server-props="dataTableServerProps" @refresh:search="getAllHits">
+                <template #top>
+                    <v-toolbar><v-toolbar-title class="text-capitalize">
+                            RefSeq
+                        </v-toolbar-title><v-spacer></v-spacer>
+
+                    </v-toolbar>
+                </template>
+                <template #[`item.accession_in_sys`]="{ item }">
+                    <CollapsibleChips :items="namesToAccessionChips(item.accession_in_sys)">
+                    </CollapsibleChips>
+                </template>
+            </ServerDbTable>
+
+
         </v-card>
 
     </v-card>
diff --git a/components/content/SystemDb.vue b/components/content/SystemDb.vue
index 571df61219336f7edf4aeaf72d54caebd1542d2b..72d1642f4e757b4da5e2a7b1881039bf534d7ec6 100644
--- a/components/content/SystemDb.vue
+++ b/components/content/SystemDb.vue
@@ -3,7 +3,7 @@ import type { SortItem } from "@/components/ServerDbTable.vue"
 import { ServerDbTable } from "#components"
 const sortBy: Ref<SortItem[]> = ref([{ key: 'title', order: "asc" }])
 const itemValue = ref("title");
-const facets: Ref<string[]> = ref(["title", "Sensor", "Activator"])
+const facets: Ref<string[]> = ref(["title", "Sensor", "Effector", "Activator", "PFAM.AC"])
 const headers: Ref<Object[]> = ref([
     { title: "System", key: "title", removable: false },
     { title: "Article", key: "doi", removable: false },
diff --git a/content/2.general-concepts/0.index.md b/content/2.general-concepts/0.index.md
index 63eb224f507b107fceb7b066ac7b8f3f57c37a98..d8f88168c00b82d6987e3c94930238fc273177f5 100644
--- a/content/2.general-concepts/0.index.md
+++ b/content/2.general-concepts/0.index.md
@@ -9,11 +9,11 @@ In the following pages are presented different general concepts that are useful
 
 You'll find information on :
 
-1. [Abortive infection](/general-concepts/abortive-infection/)
-2. [Defense Islands  ](/general-concepts/defense-islands/)
-3. [Triggers of defense systems](/general-concepts/defense-systems_trigger/)
-4. [Effectors of defense systems](/general-concepts/defense-systems_effector/)
-5. [How defense systems were and are discovered](/general-concepts/defense-systems-discovery/)
-6. [Defensive domains](/general-concepts/defensive-domains/)
-7. [MGE and defense systems](/general-concepts/mge-defense-systems/)
-8. [Anti defense systems](/general-concepts/anti-defense-systems/)
\ No newline at end of file
+1. [Abortive infection](/general-concepts/abortive-infection)
+2. [Defense Islands](/general-concepts/defense-islands)
+3. [Triggers of defense systems](/general-concepts/defense-systems_trigger)
+4. [Effectors of defense systems](/general-concepts/defense-systems_effector)
+5. [How defense systems were and are discovered](/general-concepts/defense-systems-discovery)
+6. [Defensive domains](/general-concepts/defensive-domains)
+7. [MGE and defense systems](/general-concepts/mge-defense-systems)
+8. [Anti defense systems](/general-concepts/anti-defense-systems)
\ No newline at end of file
diff --git a/content/2.general-concepts/1.abortive-infection.md b/content/2.general-concepts/1.abortive-infection.md
index e549c003f10b6cc8e21b837dea794d919e7ab261..44d6b82a1c48494e28ac1877bbe2ebf85e33984b 100644
--- a/content/2.general-concepts/1.abortive-infection.md
+++ b/content/2.general-concepts/1.abortive-infection.md
@@ -20,7 +20,15 @@ relevantAbstracts:
 ---
 
 
-The term abortive infection was coined in the 1950s :ref{doi=10.1128/jb.68.1.36-42.1954} to describe the observations that a fraction of the bacterial population did not support phage replication. This phenomenon, also called phage exclusion, was identified in multiple systems across the following decades :ref{doi=10.1016/0006-3002(61)90455-3,10.1016/0022-2836(68)90078-8,10.1128/jvi.4.2.162-168.1969,10.1128/jvi.13.4.870-880.1974} and reviewed extensively :ref{doi=10.1128/mr.45.1.52-71.1981,10.3168/jds.S0022-0302(90)78904-7,10.1111/j.1365-2958.1995.tb02255.x}. In the following years, and through the resolution of molecular mechanisms of key defense systems such as Rex or Lit, abortive infection became synonymous with infection-induced controlled cell-death. Controlled cell death upon detection of the phage infection stops the propagation of the phage and protects the rest of the bacterial population :ref{doi=10.1016/S0960-9822(00)00124-X,10.1016/j.mib.2005.06.006}. Abortive infection can thus be thought of as a form of bacterial altruism.
+The term abortive infection was coined in the 1950s :ref{doi=10.1128/jb.68.1.36-42.1954} 
+to describe the observations that a fraction of the bacterial population did not support phage replication. 
+This phenomenon, also called phage exclusion, was identified in multiple systems across the following decades 
+:ref{doi=10.1016/0006-3002(61)90455-3,10.1016/0022-2836(68)90078-8,10.1128/jvi.4.2.162-168.1969,10.1128/jvi.13.4.870-880.1974} 
+and reviewed extensively :ref{doi=10.1128/mr.45.1.52-71.1981,10.3168/jds.S0022-0302(90)78904-7,10.1111/j.1365-2958.1995.tb02255.x}. 
+In the following years, and through the resolution of molecular mechanisms of key defense systems such as Rex or Lit, abortive infection became synonymous with infection-induced controlled cell-death.
+Controlled cell death upon detection of the phage infection stops the propagation of the phage and protects the rest of the bacterial population 
+:ref{doi=10.1016/S0960-9822(00)00124-X,10.1016/j.mib.2005.06.006}. 
+Abortive infection can thus be thought of as a form of bacterial altruism.
 
 With the recent developments in phage-defense systems and microbial immunity (see :ref{doi=10.1038/s41579-023-00934-x} for a review), many newly identifed anti-phage defense systems are thought to function through abortive infection. Abortive defense systems often detect the phage infection at the later stage through protein sensing or the monitoring of host integrity but can also be based on nucleic acid sensing. Upon sensing, a diverse set of effectors can be used to reduce metabolism or induce cell-death (e.g., NAD+ depletion, translation interruption or membrane depolarisation). The diversity of and mechanisms of abortive infection were recently reviewd here :ref{doi=10.1146/annurev-virology-011620-040628}, while the evolutionary success of this paradoxical altruistic form of immunity has recently been discussed here :ref{doi=10.1016/j.mib.2023.102312}.
 
diff --git a/content/2.general-concepts/2.defense-islands.md b/content/2.general-concepts/2.defense-islands.md
index cd47beab45e15d0d3b480f58c0375c44711b9867..d012e33a0fb7ed1007afdb6ec25e91d6f7969761 100644
--- a/content/2.general-concepts/2.defense-islands.md
+++ b/content/2.general-concepts/2.defense-islands.md
@@ -11,8 +11,8 @@ contributors:
 
 # Defense Islands
 
-**Defense islands** are regions of prokaryotic genomes enriched in defense systems. Their existence first described in Makarova *et al.*:ref{doi=10.1128/JB.05535-11}, who observed that genes encoding defense systems (mainly Restriction Modification enzymes, Toxin-Antitoxin systems, but notably not CRISPR) tended to cluster preferentially on specific portions of bacterial genomes. They postulated that unknown genes commonly found associated to these regions would likely have a defensive role themselves, and confirmed bioinformatically that many of them were indeed diverged versions of classical defense systems. Other systems of genes commonly found in defense islands were later isolated and heterologously expressed to experimentally confirm to have a defensive role (BREX, DISARM). Doron *et al.*:ref{10.1126/science.aar4120}, later followed by Millmann *et al.*:ref{https://doi.org/10.1016/j.chom.2022.09.017}, used the colocalization of genes in defense islands to generate many candidate systems and test them experimentally in high throughput screens, leading to the discovery of a large number of new defense systems.
+**Defense islands** are regions of prokaryotic genomes enriched in defense systems. Their existence first described in Makarova *et al.* :ref{doi=10.1128/JB.05535-11}, who observed that genes encoding defense systems (mainly Restriction Modification enzymes, Toxin-Antitoxin systems, but notably not CRISPR) tended to cluster preferentially on specific portions of bacterial genomes. They postulated that unknown genes commonly found associated to these regions would likely have a defensive role themselves, and confirmed bioinformatically that many of them were indeed diverged versions of classical defense systems. Other systems of genes commonly found in defense islands were later isolated and heterologously expressed to experimentally confirm to have a defensive role (BREX, DISARM). Doron *et al.* :ref{doi=10.1126/science.aar4120}, later followed by Millmann *et al.* :ref{doi=10.1016/j.chom.2022.09.017}, used the colocalization of genes in defense islands to generate many candidate systems and test them experimentally in high throughput screens, leading to the discovery of a large number of new defense systems.
 
-The reasons leading to the formation and maintenance of defense islands are still unclear. Makarova *et al.*:ref{doi=10.1128/JB.05535-11} observed a that defense islands often associated with mobile genetic elements, suggesting that defense systems travel through horizontal gene transfer, taking advantage of the MGEs' mobility. This observation in itself could explain the non-random localization of defense systems in the preferred "landing pads" (=*sinks*) of mobile genetic elements. Whether the colocalization of defense systems into these islands is purely due to there horizontal transmission, or whether they reflect a deeper functional implication such as coregulation and coordination, remains debated.  
+The reasons leading to the formation and maintenance of defense islands are still unclear. Makarova *et al.* :ref{doi=10.1128/JB.05535-11} observed a that defense islands often associated with mobile genetic elements, suggesting that defense systems travel through horizontal gene transfer, taking advantage of the MGEs' mobility. This observation in itself could explain the non-random localization of defense systems in the preferred "landing pads" (=*sinks*) of mobile genetic elements. Whether the colocalization of defense systems into these islands is purely due to there horizontal transmission, or whether they reflect a deeper functional implication such as coregulation and coordination, remains debated.  
 
 
diff --git a/content/2.general-concepts/3.defense-systems_trigger.md b/content/2.general-concepts/3.defense-systems_trigger.md
index d8976494fa515b34a95a57a9d0f4b2358c5e8bcd..5e088ed2afcb2696c73054366f994eb1014ca875 100644
--- a/content/2.general-concepts/3.defense-systems_trigger.md
+++ b/content/2.general-concepts/3.defense-systems_trigger.md
@@ -7,14 +7,18 @@ layout: article
 ---
 
 # How anti-phage systems sense invading phages
+
 Upon phage infection, the bacterial immune system senses a specific phage component or modification that the phage exerts on the cell to elicit the bacterial immune response. Understanding how bacteria sense phage infection is a fundamental question, which remains unanswered for the majority of recently discovered immune systems. There are dozens of cases in which the mechanism of immunity has been elucidated, but the phage trigger remains elusive. Understanding how antiphage systems are activated is key for a full understanding of bacterial immunity and for repurposing them as molecular tools as has been done for restriction enzymes and CRISPR-Cas. 
 
 ## Diversity
+
 Various determinants of the phage can elicit bacterial immunity either in a direct or indirect manner. The most common and well known prokaryotic anti-phage systems, restriction enzymes and CRISPR-Cas, recognize and cleave phage DNA or RNA. More recently, a CBASS system has been found to directly bind to a structured phage RNA that triggers immune activation :ref{doi=10.1101/2023.03.07.531596}. In other cases, defense systems are activated by protein coding phage genes. In some cases, the phage protein is directly sensed by the defense systems, as has been beautifully demonstrated for the Avs systems that directly bind either the phage terminase or portal protein :ref{doi=10.1126/science.abm4096}. In other cases, the phage protein can be sensed indirectly by the defense system, for example by detecting its activity in the cell. Such an indirect mechanism has been found for example in the case of some retron defense systems that are triggered by phage tampering with the RecBCD protein complex :ref{doi=10.1016/j.cell.2020.09.065,10.1016/j.cell.2023.02.029}. For a comprehensive coverage of all recent phage detection mechanisms the recent review by Huiting and Bondy-Denomy :ref{doi=10.1016/j.mib.2023.102325} is highly recommended. 
 
 ## Method of discovery:
+
 The main method used to pinpoint phage components that trigger a specific defense system of interest has been through a simple classic genetics approach, whereby mutant phages that overcome the defense system are examined. Such mutants often occur spontaneously and can thus be selected for by simply picking phage plaques that are able to form on a lawn of bacteria expressing the defense system :ref{doi=10.1016/j.cell.2023.02.029,10.1016/j.mib.2023.102325}. The hypothesis is that the phage mutant escapes bacterial immunity due to a mutation in the component sensed by the system. Thus, sequencing these phage mutants and identification of the mutated locus is the first required step. To validate that the mutated phage component is indeed the actual trigger of the defense system, follow up experiments are required. For example, in some cases expression of this phage component without any other phage genes is sufficient to elicit the activity of bacterial immune system. This approach was used to identify Borvo activation by expression of the phage DNA polymerase, Dazbog activation by expression of a phage DNA methylase, retron activation by either phage SSB proteins :ref{doi=10.1016/j.cell.2023.02.029} or by proteins that inhibit the host RecBCD3, CapRel triggering by the phage Capsid protein :ref{doi=10.1038/s41586-022-05444-z} and many more :ref{doi=10.1016/j.mib.2023.102325}. Additional biochemical pulldown assays can be used to assess binding of the defense system to the suspected phage trigger. 
 One major caveat in the above approach is that in some cases mutant phages that escape the immune system cannot be isolated. This can occur for example if the defense system senses a general fold of a highly conserved and essential phage protein. In this case a simple mutation in the protein will not suffice for the phage to escape detection. In such cases, an alternative approach can be used that does not rely on isolation of escape mutants. An overexpression library of all phage genes can be co-expressed with the defense system of interest, and then assayed for immune activation. This approach was successfully applied for identification phage components that trigger diverse Avs systems :ref{doi=10.1126/science.abm4096}. 
 
-## General concepts: 
+## General concepts
+
 Although much is still unknown regarding how bacterial immune systems sense phage infection, by combining the data observed so far, several general concepts in immune sensing are beginning to come to light. First, mechanistically diverse immune systems appear to have converged to sense common conserved phage components4.  These include the phage core replication machinery, host takeover machinery and structural components. Second, several studies have found cases in which defense occurs in a multi-layered fashion, whereby a second system is activated when the first one fails  :ref{doi=10.1016/j.cell.2020.09.065,10.1016/j.chom.2022.02.018,10.1006/jmbi.1995.0343}. Research in upcoming years is expected to reveal additional guiding principles in the ways bacteria detect phages. 
diff --git a/content/2.general-concepts/6.defensive-domains.md b/content/2.general-concepts/6.defensive-domains.md
index d645fa58ecf4233fdcc6a091975d5e4b251a5660..44960e31f74bd4b074e10d1feff9797832a35945 100644
--- a/content/2.general-concepts/6.defensive-domains.md
+++ b/content/2.general-concepts/6.defensive-domains.md
@@ -19,4 +19,5 @@ To examplify this idea, the figure is a depiction of the ThsA protein involved i
 Although a considerable diversity of molecular mechanisms have been described for defense systems, it is striking to observe that some functional domains are recurrently involved in antiphage defense :ref{doi=10.1038/s41586-021-04098-7}. When studying the presence of a new defense system, the *in silico* characterization of the domains present in the system can provide valuable information regarding the molecular mechanism of the system. If one protein of the system contains for example a TerB domain, this might indicate that the system is involved in membrane integrity surveillance as this domain was previously shown to be associated with the periplasmic membrane :ref{doi=10.1016/j.chom.2022.09.017}. If a protein of the system contains a TIR domain this might indicate that the system possess a NAD degradation activity or that the protein could multimerize as both functions have been shown for this domain in the past :ref{doi=10.3389/fimmu.2021.784484}. 
 
 # Domains can be conserved throughout evolution
+
 It is clear that some defense systems can be conserved among different clades of bacteria but it was also observed that the unit of evolutionary conservation can be the protein domain :ref{doi=10.1038/s41467-022-30269-9}. As a consequence, it is frequent to find the same domain associated with a wide range of distinct other domains in different defense systems :ref{doi=10.1016/j.mib.2023.102312}. This is well illustrated by defense systems such [Avs](/defense-systems/avs) or [CBASS](/defense-systems/cbass) that can be constituted of diverse effector proteins which differ from each other based on the specific domains that compose them :ref{doi=10.1126/science.aba0372}, :ref{doi=10.1038/s41564-022-01239-0}, :ref{doi=10.1038/s41564-020-0777-y}. The modular aspect of protein domains fits with the concept of "evolution as tinkering" stating that already existing objects (here protein domains) can often be repurposed in new manners, allowing the efficient development of novel functions :ref{doi=10.1126/science.860134}.
diff --git a/content/2.general-concepts/8.anti-defense-systems.md b/content/2.general-concepts/8.anti-defense-systems.md
index b8ef53112da6402c6a08f083088cc0571f6d81e2..d743a668c59cc7cce51d7c54143ddff7029a1486 100644
--- a/content/2.general-concepts/8.anti-defense-systems.md
+++ b/content/2.general-concepts/8.anti-defense-systems.md
@@ -26,12 +26,10 @@ Bacteria can hide receptors behind surface structures such as extracellular poly
 
 Bacteria encode a variety of defense systems that prevent phage infection from progressing in various ways. Despite all this variability, all bacterial defense systems are schematically composed of three parts: a sensor recognizing the infection, an effector that achieves protection and a way to transmit the information between the sensor and the effector, either through signaling molecules or protein-protein interactions. Phage anti-defense proteins can target all three of these components.
 - Sensor targeting:
-
 	- Competitive binding to the sensor: an anti-DSR2 protein from phages phi3T and SPbeta can bind the bacterial DSR2 protein and prevent the physical interaction between DSR2 and its phage activator, the tail tube protein :ref{doi=10.1038/s41564-022-01207-8}. Moreover, Ocr protein from T7 can mimic a B-form DNA oligo and acts as a competitive inhibitor of bacterial type I restriction modification systems :ref{doi=10.1016/s1097-2765(02)00435-5}.
 	- Masking the activator: some jumbo phages are able to produce a nucleus-like proteinaceous structure that hides phage DNA and replication machinery away from DNA-targeted systems such as type I CRISPR system :ref{doi=10.1038/s41564-019-0612-5}.
 
 - Transmission targeting:
-
 	- Degradation of signaling molecules: many systems rely on the production of a nucleotidic signaling molecule after phage sensing to activate the effector such as Pycsar, CBASS, and Thoeris systems. Phages possess proteins that can degrade these molecules to prevent effector activation, such as the anti CBASS Acb1 from phage T4 and the anti Pycsar Apyc1 from phage SBSphiJ :ref{doi=10.1038/s41586-022-04716-y}.
     - Sequestration of signaling molecules: an alternative strategy is to bind the signaling molecule very tightly without degrading it, which still prevents effector activation but is presumably easier to evolve than a catalysis-dependent degradation. These phage proteins are called sponges, and two were identified as anti-Thoeris: Tad1 from phage SBSphiJ7 and Tad2 from phage SPO1 and SPO1L3 :ref{doi=10.1038/s41586-022-05375-9,10.1038/s41586-023-06869-w}.
 
diff --git a/content/2.general-concepts/9.defense-systems-effectors.md b/content/2.general-concepts/9.defense-systems-effectors.md
new file mode 100644
index 0000000000000000000000000000000000000000..675f952135b53a54c3459ca38e5f25b2cab8fe56
--- /dev/null
+++ b/content/2.general-concepts/9.defense-systems-effectors.md
@@ -0,0 +1,41 @@
+---
+title: DefenseFinder effectors
+layout: article
+relevantAbstracts:
+  - doi: 10.1038/s41579-023-00934-x
+contributors:
+  - Héloïse Georjon
+---
+
+# Defense systems effectors
+
+Most of the anti-phage defense systems of bacteria can be described as a combination of two main components. 
+First, a sensing component that detects phage infection to trigger the immune response 
+(see [defense-systems_trigger](/general-concepts/defense-systems_trigger/)). 
+Second, an effector component that mediates the immune response following the detection of phage infection.
+
+The effector components of anti-phage systems are very diverse, and can be arbitrarily distributed in broad categories :ref{doi=10.1038/s41579-023-00934-x} :
+
+## Nucleic-acid-degrading effectors.
+
+Many defense systems target (either through cleavage or modification) nucleic acids to mediate the immune response. 
+These nucleic acids targeting systems are divided between systems that specifically target phage nucleic acids to stop 
+phage replication, and systems that untargetedly affect bacterial and viral nucleic acids to halt the growth of both the 
+infected host and the phage. 
+Nucleic-acid-degrading systems include [RM](/defense-systems/rm), [CRISPR-Cas](/defense-systems/cas), [Ssp](/defense-systems/sspbcde) and [Ddn](/defense-systems/dnd), certain types of [CBASS](/defense-systems/cbass), [Avs](/defense-systems/avs) and [Lamassu](/defense-systems/lamassu-fam), [PrrC](/defense-systems/prrc), [RloC](/defense-systems/rloc)...
+
+## Nucleotide-modifying effectors.
+
+Other types of defense systems target the nucleotide pool of the infected cell. 
+For instance, Viperins produce modified nucleotides that inhibit phage transcription; defensive dCTP deaminases and dGTPases respectively 
+degrade CTP and GTP to halt phage infection;  [Thoeris](/defense-systems/thoeris), [DSR](/defense-systems/dsr) and certain types of [pAgo](/defense-systems/pago) and [CBASS](/defense-systems/cbass) degrade NAD+ to cause growth arrest of the infected host.
+
+## Membrane-disrupting effectors.
+
+Many defense systems encode proteins that disrupt the membrane integrity of the infected cell 
+(by opening pores, targeting the membrane phospholipids or through transmembrane domains), leading to growth arrest.
+They include for instance bacterial Gasdermins, RexAB, Pif, AbiZ, certain types of [pAgo](/defense-systems/pago), [retrons](/defense-systems/retron), [CBASS](/defense-systems/cbass), [PYCSAR](/defense-systems/pycsar) and [Avs](/defense-systems/avs) systems.
+
+## Other types of effectors.
+
+Finally, some types of less prevalent effectors were not included into these broad categories. This includes protein modifying effectors, and some chemical defense systems.
diff --git a/content/2.general-concepts/defense-systems-effectors.md b/content/2.general-concepts/defense-systems-effectors.md
deleted file mode 100644
index 65c8b9fcd7d407ad6c5c57a90dc1ab5ba7d71239..0000000000000000000000000000000000000000
--- a/content/2.general-concepts/defense-systems-effectors.md
+++ /dev/null
@@ -1,31 +0,0 @@
----
-title: DefenseFinder effectors
-layout: article
-relevantAbstracts:
-  - doi: 10.1038/s41579-023-00934-x
-contributors:
-  - Héloïse Georjon
----
-
-# Defense systems effectors
-
-Most of the anti-phage defense systems of bacteria can be described as a combination of two main components. First, a sensing component that detects phage infection to trigger the immune response (see [defense-systems_trigger](/general-concepts/defense-systems_trigger/)). Second, an effector component that mediates the immune response following the detection of phage infection.
-
-The effector components of anti-phage systems are very diverse, and can be arbitrarily distributed in broad categories :ref{doi=10.1038/s41579-023-00934-x} :
-
-## Nucleic-acid-degrading effectors.
-
-Many defense systems target (either through cleavage or modification) nucleic acids to mediate the immune response. These nucleic acids targeting systems are divided between systems that specifically target phage nucleic acids to stop phage replication, and systems that untargetedly affect bacterial and viral nucleic acids to halt the growth of both the infected host and the phage. 
-Nucleic-acid-degrading systems include [RM](/defense-systems/RM), [CRISPR-Cas](/defense-systems/Cas), [Ssp](defense-systems/sspbcde) and [Ddn](defense-systems/dnd), certain types of [CBASS](/defense-systems/cbass), [Avs](/defense-systems/avs) and [Lamassu](/defense-systems/lamassu-fam), [PrrC](/defense-systems/prrc), [RloC](/defense-systems/rloc)...
-
-## Nucleotide-modifying effectors.
-
-Other types of defense systems target the nucleotide pool of the infected cell. For instance, Viperins produce modified nucleotides that inhibit phage transcription; defensive dCTP deaminases and dGTPases respectively degrade CTP and GTP to halt phage infection;  [Thoeris](/defense-systems/thoeris), [DSR](/defense-systems/dsr) and certain types of [pAgo](/defense-systems/pago) and [CBASS](/defense-systems/cbass) degrade NAD+ to cause growth arrest of the infected host.
-
-## Membrane-disrupting effectors.
-
-Many defense systems encode proteins that disrupt the membrane integrity of the infected cell (by opening pores, targeting the membrane phospholipids or through transmembrane domains), leading to growth arrest. They include for instance bacterial Gasdermins, RexAB, Pif, [AbiZ](), certain types of [pAgo](/defense-systems/pago), [retrons](/defense-systems/retron), [CBASS](/defense-systems/cbass), [PYCSAR](/defense-systems/pycsar) and [Avs](/defense-systems/avs) systems.
-
-## Other types of effectors.
-
-Finally, some types of less prevalent effectors were not included into these broad categories. This includes protein modifying effectors, and some chemical defense systems.
diff --git a/content/3.defense-systems/pago.md b/content/3.defense-systems/pago.md
index 9dd7d2049b551bfd315787f71b06ea2c6f6eba97..7028073c44274bcd28fc38775cfe0063145692ed 100644
--- a/content/3.defense-systems/pago.md
+++ b/content/3.defense-systems/pago.md
@@ -5,14 +5,59 @@ tableColumns:
     article:
       doi: 10.1186/1745-6150-4-29
       abstract: |
-        BACKGROUND: In eukaryotes, RNA interference (RNAi) is a major mechanism of defense against viruses and transposable elements as well of regulating translation of endogenous mRNAs. The RNAi systems recognize the target RNA molecules via small guide RNAs that are completely or partially complementary to a region of the target. Key components of the RNAi systems are proteins of the Argonaute-PIWI family some of which function as slicers, the nucleases that cleave the target RNA that is base-paired to a guide RNA. Numerous prokaryotes possess the CRISPR-associated system (CASS) of defense against phages and plasmids that is, in part, mechanistically analogous but not homologous to eukaryotic RNAi systems. Many prokaryotes also encode homologs of Argonaute-PIWI proteins but their functions remain unknown. RESULTS: We present a detailed analysis of Argonaute-PIWI protein sequences and the genomic neighborhoods of the respective genes in prokaryotes. Whereas eukaryotic Ago/PIWI proteins always contain PAZ (oligonucleotide binding) and PIWI (active or inactivated nuclease) domains, the prokaryotic Argonaute homologs (pAgos) fall into two major groups in which the PAZ domain is either present or absent. The monophyly of each group is supported by a phylogenetic analysis of the conserved PIWI-domains. Almost all pAgos that lack a PAZ domain appear to be inactivated, and the respective genes are associated with a variety of predicted nucleases in putative operons. An additional, uncharacterized domain that is fused to various nucleases appears to be a unique signature of operons encoding the short (lacking PAZ) pAgo form. By contrast, almost all PAZ-domain containing pAgos are predicted to be active nucleases. Some proteins of this group (e.g., that from Aquifex aeolicus) have been experimentally shown to possess nuclease activity, and are not typically associated with genes for other (putative) nucleases. Given these observations, the apparent extensive horizontal transfer of pAgo genes, and their common, statistically significant over-representation in genomic neighborhoods enriched in genes encoding proteins involved in the defense against phages and/or plasmids, we hypothesize that pAgos are key components of a novel class of defense systems. The PAZ-domain containing pAgos are predicted to directly destroy virus or plasmid nucleic acids via their nuclease activity, whereas the apparently inactivated, PAZ-lacking pAgos could be structural subunits of protein complexes that contain, as active moieties, the putative nucleases that we predict to be co-expressed with these pAgos. All these nucleases are predicted to be DNA endonucleases, so it seems most probable that the putative novel phage/plasmid-defense system targets phage DNA rather than mRNAs. Given that in eukaryotic RNAi systems, the PAZ domain binds a guide RNA and positions it on the complementary region of the target, we further speculate that pAgos function on a similar principle (the guide being either DNA or RNA), and that the uncharacterized domain found in putative operons with the short forms of pAgos is a functional substitute for the PAZ domain. CONCLUSION: The hypothesis that pAgos are key components of a novel prokaryotic immune system that employs guide RNA or DNA molecules to degrade nucleic acids of invading mobile elements implies a functional analogy with the prokaryotic CASS and a direct evolutionary connection with eukaryotic RNAi. The predictions of the hypothesis including both the activities of pAgos and those of the associated endonucleases are readily amenable to experimental tests.
+        BACKGROUND: In eukaryotes, RNA interference (RNAi) is a major mechanism of defense against viruses and transposable elements as well of regulating translation of endogenous mRNAs. 
+        The RNAi systems recognize the target RNA molecules via small guide RNAs that are completely or partially complementary to a region of the target. 
+        Key components of the RNAi systems are proteins of the Argonaute-PIWI family some of which function as slicers, 
+        the nucleases that cleave the target RNA that is base-paired to a guide RNA. 
+        Numerous prokaryotes possess the CRISPR-associated system (CASS) of defense against phages and plasmids that is, in part, 
+        mechanistically analogous but not homologous to eukaryotic RNAi systems. 
+        Many prokaryotes also encode homologs of Argonaute-PIWI proteins but their functions remain unknown. 
+        RESULTS: We present a detailed analysis of Argonaute-PIWI protein sequences and the genomic neighborhoods of the respective genes in prokaryotes. 
+        Whereas eukaryotic Ago/PIWI proteins always contain PAZ (oligonucleotide binding) and PIWI (active or inactivated nuclease) domains, the prokaryotic Argonaute homologs (pAgos) fall into two major groups in which the PAZ domain is either present or absent. The monophyly of each group is supported by a phylogenetic analysis of the conserved PIWI-domains. Almost all pAgos that lack a PAZ domain appear to be inactivated, and the respective genes are associated with a variety of predicted nucleases in putative operons. An additional, uncharacterized domain that is fused to various nucleases appears to be a unique signature of operons encoding the short (lacking PAZ) pAgo form. By contrast, almost all PAZ-domain containing pAgos are predicted to be active nucleases. Some proteins of this group (e.g., that from Aquifex aeolicus) have been experimentally shown to possess nuclease activity, and are not typically associated with genes for other (putative) nucleases. Given these observations, the apparent extensive horizontal transfer of pAgo genes, and their common, statistically significant over-representation in genomic neighborhoods enriched in genes encoding proteins involved in the defense against phages and/or plasmids, we hypothesize that pAgos are key components of a novel class of defense systems. The PAZ-domain containing pAgos are predicted to directly destroy virus or plasmid nucleic acids via their nuclease activity, whereas the apparently inactivated, PAZ-lacking pAgos could be structural subunits of protein complexes that contain, as active moieties, the putative nucleases that we predict to be co-expressed with these pAgos. All these nucleases are predicted to be DNA endonucleases, so it seems most probable that the putative novel phage/plasmid-defense system targets phage DNA rather than mRNAs. Given that in eukaryotic RNAi systems, the PAZ domain binds a guide RNA and positions it on the complementary region of the target, we further speculate that pAgos function on a similar principle (the guide being either DNA or RNA), and that the uncharacterized domain found in putative operons with the short forms of pAgos is a functional substitute for the PAZ domain. CONCLUSION: The hypothesis that pAgos are key components of a novel prokaryotic immune system that employs guide RNA or DNA molecules to degrade nucleic acids of invading mobile elements implies a functional analogy with the prokaryotic CASS and a direct evolutionary connection with eukaryotic RNAi. The predictions of the hypothesis including both the activities of pAgos and those of the associated endonucleases are readily amenable to experimental tests.
     Sensor: Detecting invading nucleic acid
     Activator: Direct
     Effector: Diverse (Nucleotide modifyingn, Membrane disrupting)
     PFAM: PF02171, PF13289, PF13676, PF14280, PF18742
+contributors:
+  - Daan Swarts
+relevantAbstracts:
+  - doi: 10.1016/j.cell.2022.03.012
+  - doi: 10.1016/j.chom.2022.04.015
+  - doi: 10.1038/s41564-022-01207-8
+  - doi: 10.1038/s41586-020-2605-1
+  - doi: 10.1186/1745-6150-4-29
+  - doi: 10.1038/s41564-022-01239-0
 ---
 
 # pAgo
+
+## Description
+Argonaute proteins comprise a diverse protein family and can be found in both prokaryotes and eukaryotes :ref{doi=10.1016/j.mib.2023.102313}. Despite low sequence conservation, eAgos and long pAgos generally have a conserved domain architecture and share a common mechanism of action; they use a 5'-phosphorylated single stranded nucleic acid guide (generally 15-22 nt in length) to target complementary nucleic acid sequences :ref{doi=10.1038/nsmb.2879} eAgos strictly mediate RNA-guided RNA silencing, while pAgos show higher mechanistic diversification, and can make use of guide RNAs and/or single-stranded guide DNAs to target RNA and/or DNA targets :ref{doi=10.1016/j.mib.2023.102313}. Depending on the presence of catalytic residues and the degree of complementarity between the guide and target sequences, eAgo and pAgos either cleave the target, or recruit and/or activate accessory proteins. This can result in degradation of the target nucleic acid, but might also trigger alternative downstream effects, ranging from poly(A) tail shortening and RNA decapping :ref{doi=10.1016/J.CELL.2018.03.006} or chromatin formation in eukaryotes :ref{doi=10.1038/s41580-022-00528-0}, to abortive infection in prokaryotes :ref{doi=10.1016/j.tcb.2022.10.005}.
+
+## Molecular mechanism
+
+Based on their phylogeny, Agos have been subdivided in various (sub)clades. eAgos are generally subdivided in the AGO and PIWI clades, but these will not be discussed further here. pAgos can be further subdivided in long-A pAgos, long-B pAgos, short pAgos, SiAgo-like pAgos, and PIWI-RE proteins :ref{doi=10.1128/mBio.01935-18,10.1016/j.mib.2023.102313,10.1016/j.tcb.2022.10.005,10.1186/1745-6150-8-13,10.1186/1745-6150-4-29}. Below, we briefly outline the general mechanism of pAgos that have a demonstrated role in host defense.
+
+### Long-A pAgos
+Akin to eAgos, most long A-pAgos characterized to date have a N-L1-PAZ-L2-MID-PIWI domain architecture :ref{doi=10.1038/nsmb.2879}. In contrast to eAgos, however, certain long-A pAgos use a single stranded guide DNA to bind and cleave complementary target DNA sequences :ref{doi=10.1093/nar/gkz306,10.1093/nar/gkz379,10.1038/s41586-020-2605-1,10.1093/nar/gkv415,10.1038/nature12971,10.1038/nmicrobiol.2017.35}. Long-A pAgos are preferentially programmed with guide DNAs targeting invading DNA through a poorly understood mechanism, which might involve DNA repair proteins :ref{doi=10.1038/s41586-020-2605-1} or the pAgo itself :ref{doi=10.1016/j.molcel.2017.01.033,10.1038/nmicrobiol.2017.34}. Most long-A pAgos have an intact catalytic site in the PIWI domain which allows to cleave their targets :ref{doi=10.1073/pnas.1321032111}. As such, they act as an innate immune system that clear plasmid and phage DNA from the cell :ref{doi=10.1093/nar/gkz379,10.1038/s41586-020-2605-1,10.1093/nar/gkv415,10.1038/nature12971,10.1093/nar/gkad290}. 
+
+Within the long-A pAgo clade various subclades of other pAgos exist that rely on distinct function mechanisms. For example, various long-A pAgo can (additionally) use guide RNAs and/or cleave RNA targets. Furthermore, CRISPR-associated pAgos use 5'-OH guide RNAs to target DNA :ref{doi=10.1073/pnas.1524385113}, and PliAgo-like pAgos use small DNA guides to target RNA :ref{doi=10.1038/s41467-022-32079-5}. Certain long-A pAgos genetically co-localize with other putative enzymes including (but not limited to) putative nucleases, helicases, DNA-binding proteins, or PLD-like proteins :ref{doi=10.1038/nsmb.2879,10.1128/mBio.01935-18}. The relevance of these associations is currently unknown. 
+
+### Long-B pAgos
+Akin to long-A pAgogs, long B-pAgos have a N-L1-PAZ-L2-MID-PIWI domain composition, but most have a shorter PAZ* domain, and in contrast to long-A pAgos all long-B pAgos are catalytically inactive :ref{doi=10.1128/mBio.01935-18}. Long-B pAgos characterized to date use guide RNAs to bind invading DNA :ref{doi=10.1038/s41598-023-32600-w,10.1016/j.molcel.2013.08.014,10.1038/s41467-023-42793-3}. In absence of co-encoded proteins, long-B pAgos repress invader activity :ref{doi=10.1016/j.molcel.2013.08.014}. In addition, most long-B pAgos are co-encoded with effector proteins including (but not limited to) SIR2, nucleases, membrane proteins, and restriction endonucleases :ref{doi=10.1038/nsmb.2879,10.1128/mBio.01935-18,10.1186/1745-6150-4-29,10.1038/s41467-023-42793-3}. These effector proteins are activated upon pAgo-mediated invader detection, and generally catalyze reactions that result in cell death :ref{doi=10.1038/s41467-023-42793-3}. As such, long-B pAgo together with their associated proteins mediate abortive infection. 
+
+### Short pAgos
+Short pAgos are truncated: they only contain the MID and PIWI domains essential for guide-mediate target binding :ref{doi=10.1016/j.tcb.2022.10.005}. They are catalytically inactive and are co-encoded with an APAZ domain that is fused to one of various effector domains. In short pAgo systems characterized to date, the short pAgo and the APAZ domain-containing protein form a heterodimeric complex :ref{doi=10.1016/j.cell.2022.03.012,10.1038/s41564-022-01239-0}. Within this complex, the short pAgo uses a guide RNA to bind complementary target DNAs. This triggers catalytic activation of the effector domain fused to the APAZ domain, generally resulting in cell death :ref{doi=10.1016/j.cell.2022.03.012,10.1038/s41564-022-01239-0}. As such, short pAgo systems mediate abortive infection. 
+
+Based on their phylogeny, short pAgos are subdivided in S1A, S1B, S2A, and S2B clades :ref{doi=10.1128/mBio.01935-18,10.1016/j.tcb.2022.10.005}. In clade S1A and S1B (SPARSA) systems, APAZ is fused to an SIR2 domain. In clade S2A (SPARTA) systems, APAZ is fused to a TIR domain. Both SPARSA and SPARTA systems trigger cell death by depletion of NAD(P)+  :ref{doi=10.1016/j.cell.2022.03.012,10.1038/s41564-022-01239-0}. In S2B clade systems, APAZ is fused to one or more effector domains, including Mrr-like, DUF4365, RecG/DHS-like and other domains. In all clade S1A SPARSA systems, but also for certain other systems within other clades, the effector-APAZ is fused to the short pAgo. 
+
+### Pseudo-short pAgos
+Akin to short pAgos, pseudo-short pAgos are comprised of the MID and PIWI domains only :ref{doi=10.1016/j.tcb.2022.10.005}. However, they do not phylogenetically cluster with canonical short pAgos and do not colocalize with effector-APAZ proteins. Instead, certain pseudo-short are found across the long-A and long-B pAgo clades (e.g. Archaeoglobus fulgidus pAgo, a truncated long-B pAgo :ref{doi=10.1038/s41598-023-32600-w,10.1038/s41598-021-83889-4}), while others form a distinct branch in the phylogenetic pAgo tree (see SiAgo-like pAgos below).  
+
+### SiAgo-like pAgos
+SiAgo-like pAgos are pseudo-short pAgos that form an separate branch in the phylogenetic tree of pAgos. They are named after the type system from Sulfolobus islandicus :ref{doi=10.1016/j.chom.2022.04.015}. SiAgo is comprised of MID and PIWI domains, and is co-encoded with Ago associated proteins Aga1 and Aga2. SiAgo and Aga1 form a cytoplasmic heterodimeric complex. While it is currently unknown what guide/target types activate the SiAgo/Aga1 complex, it is directed toward membrane-localized Aga2 upon viral infection. This triggers Aga2-mediated membrane depolarization and causes cell death :ref{doi=10.1016/j.chom.2022.04.015}. 
+
+
 ## Example of genomic structure
 
 A total of 6 subsystems have been described for the pAgo system.
@@ -224,18 +269,4 @@ end
     style Title3 fill:none,stroke:none,stroke-width:none
     style Title4 fill:none,stroke:none,stroke-width:none
 </mermaid>
-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
-    - doi: 10.1016/j.cell.2022.03.012
-    - doi: 10.1016/j.chom.2022.04.015
-    - doi: 10.1038/s41564-022-01207-8
-    - doi: 10.1038/s41586-020-2605-1
-    - doi: 10.1186/1745-6150-4-29
-    - doi: 10.1038/s41564-022-01239-0
-
----
-::
 
diff --git a/packages/df-wiki-cli/df_wiki_cli/meilisearch/__init__.py b/packages/df-wiki-cli/df_wiki_cli/meilisearch/__init__.py
index ed3c00314fca625864f9c24a22e41dead0ce4414..b3ec461a9fc5d686aae9b8b60c4f63c03e7a87b2 100644
--- a/packages/df-wiki-cli/df_wiki_cli/meilisearch/__init__.py
+++ b/packages/df-wiki-cli/df_wiki_cli/meilisearch/__init__.py
@@ -149,7 +149,7 @@ def update_structure(
     )
     print(pagination_settings_task)
     attr_task = index.update_filterable_attributes(
-        body=["system", "completed", "prediction_type"]
+        body=["system", "completed", "prediction_type", "plddts", "iptm+ptm", "pDockQ"]
     )
     params = {
         "maxValuesPerFacet": 1000000,